Evidence map›Paper›PMID 15075277›Full record

ArticleEukaryotic cell2004

Cryptosporidium parvum mitochondrial-type HSP70 targets homologous and heterologous mitochondria.

Jan Slapeta, Janet S Keithly

Open access · diamondAbstract read
In one paragraph

Article in Eukaryotic cell, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
5.3field-weighted citation impact, top 4% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

13 citing papers in PubMed, 61 citations in OpenAlex.

  1. The history of cryptosporidiosis.Parasites & vectors · 2026
    Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Diversity and reductive evolution of mitochondria among microbial eukaryotes.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2010
    Review
  7. Review
  8. Review
  9. Article
  10. The structural and functional diversity of Hsp70 proteins from Plasmodium falciparum.Protein science : a publication of the Protein Society · 2007
    Review
  11. Article
  12. Article
  13. Multiple secondary origins of the anaerobic lifestyle in eukaryotes.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2006
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 2 institutions in 1 country.

Jan SlapetaWadsworth Center, New York State Department of Health, Albany, New York 12201-2002, USA. jan.slapeta@ese.u-psud.fr
Janet S Keithly
New York State Department of Health · USWadsworth Center · US

Funding

TB TRAINING &RESEARCH PROGRAMD43TW000915 · FIC · WADSWORTH CENTER · PI MORSE, DALE L · 1997 to 2001
$1.0M
FIC NIH HHS D43 TW000915FIC NIH HHS TW00915-05
6 · The paper itself

Abstract

A mitochondrial HSP70 gene (Cp-mtHSP70) is described for the apicomplexan Cryptosporidium parvum, an agent of diarrhea in humans and animals. Mitochondrial HSP70 is known to have been acquired from the proto-mitochondrial endosymbiont. The amino acid sequence of Cp-mtHSP70 shares common domains with mitochondrial and proteobacterial homologues, including 34 amino acids of an NH2-terminal mitochondrion-like targeting presequence. Phylogenetic reconstruction places Cp-mtHSP70 within the mitochondrial clade of HSP70 homologues. Using reverse transcription-PCR, Cp-mtHSP70 mRNA was observed in C. parvum intracellular stages cultured in HCT-8 cells. Polyclonal antibodies to Cp-mtHSP70 recognize a approximately 70-kDa protein in Western blot analysis of sporozoite extracts. Both fluorescein- and immunogold-labeled anti-Cp-mtHSP70 localize to a single mitochondrial compartment in close apposition to the nucleus. Furthermore, the NH2-terminal presequence of Cp-mtHSP70 can correctly target green fluorescent protein to the single mitochondrion of the apicomplexan Toxoplasma gondii and the mitochondrial network of the yeast Saccharomyces cerevisiae. When this presequence was truncated, the predicted amphiphilic alpha-helix was shown to be essential for import into the yeast mitochondrion. These data further support the presence of a secondarily reduced relict mitochondrion in C. parvum.

Indexed as

Amino Acid SequenceAnimalsCryptosporidium parvumEscherichia coli ProteinsGene ExpressionHSP70 Heat-Shock ProteinsMicroscopy, Electron, TransmissionMicroscopy, FluorescenceMitochondriaMolecular Sequence DataPhylogenyProtein Sorting SignalsProtein Structure, SecondaryProtein TransportSequence AlignmentSporozoitesdnaK protein, E coliEscherichia coli ProteinsHSP70 Heat-Shock ProteinsProtein Sorting Signals

Identifiers

PMID15075277
PMCPMC387664
OpenAlexW2141455079

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.